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Information on EC 3.4.21.120 - oviductin
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3.4.21.120 oviductinSpecify your search results
Word Map
- 3.4.21.120
- fetal
- cirrhosis
- pregnancy
-
resect
- chorionic
- albumin
- women
- hepatocytes
- gonadotropin
-
ultrasound
- amniotic
-
carcinoembryonic
-
tomography
-
prenatal
-
postoperative
- metastases
- abdominal
-
preoperative
- yolk
-
portal
-
trimester
-
ultrasonography
- testicular
-
curative
- teratoma
-
amniocentesis
-
hepatectomy
-
child-pugh
-
cytokeratins
-
intrahepatic
- endoderm
-
chemoembolization
- estriol
- hepatoblastomas
-
unconjugated
- prothrombin
-
unresectable
-
milan
- trisomy
-
transarterial
-
hbsag
-
transcatheter
- seminoma
-
orchiectomy
-
spina
- culinaris
-
barcelona
-
radiofrequency
- papp-a
-
nuchal
The enzyme appears in viruses and cellular organisms
Reaction Schemes
preferential cleavage at Gly-Ser-Arg373-/- of glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41
Synonyms
alpha-fetoprotein, oviductin, ovochymase, oviductin-1, oviductin-i, oviductal protease, ovochymase 2, gp43 processing protease, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-fetoprotein
-
human oviductin (hOV-I) and human alpha-fetoprotein (hAFP) are chemically similar and immunologically identical molecules
hAFP
-
human oviductin (hOV-I) and human alpha-fetoprotein (hAFP) are chemically similar and immunologically identical molecules
hOV-1
-
human oviductin (hOV-I) and human alpha-fetoprotein (hAFP) are chemically similar and immunologically identical molecules
oviductal protease
oviductin
oviductin-I
ovochymase 2
oviductin-I
-
human oviductin (hOV-I) and human alpha-fetoprotein (hAFP) are chemically similar and immunologically identical molecules
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
preferential cleavage at Gly-Ser-Arg373-/- of glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41
-
-
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
55 kDa glycoprotein + H2O
?
-
the oviductal protease selectively hydrolyzes in vitro the 84 kDa and the 55 kDa glycoproteins of the coelomic envelope
-
-
?
84 kDa glycoprotein + H2O
?
-
the oviductal protease selectively hydrolyzes in vitro the 84 kDa and the 55 kDa glycoproteins of the coelomic envelope
-
-
?
Nalpha-tert-butoxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumarin-7-amide + H2O
Nalpha-tert-butoxycarbonyl-Leu-Ser-Thr-Arg + 7-amino-4-methylcoumarin
-
14% of the activity with Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide
-
-
?
Nalpha-tert-butoxycarbonyl-Leu-Thr-Arg-4-methylcoumarin-7-amide + H2O
Nalpha-tert-butoxycarbonyl-Leu-Thr-Arg + 7-amino-4-methylcoumarin
-
12% of the activity with Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide
-
-
?
Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide + H2O
Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Nalpha-tert-butoxycarbonylphenylalanylserylarginyl-7-amido-4-methylcoumarin + H2O
Nalpha-tert-butoxycarbonylphenylalanylserylarginine + 7-amino-4-methylcoumarin
-
-
-
-
?
Pro-Phe-Arg-4-methylcoumarin-7-amide + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
9% of the activity with Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide
-
-
?
Pyr-Gly-Arg-4-methylcoumarin-7-amide + H2O
Pyr-Gly-Arg + 7-amino-4-methylcoumarin
-
9% of the activity with Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide
-
-
?
additional information
?
-
-
it is proposed that hamster oviductin is a mucin-type glycoprotein which might act as a protective secretion influencing the first steps of the reproductive process necessary for the normal triggering of fertilization and early embryonic development
-
-
?
gp43 + H2O
gp41 + ?
oviductin alone is the oviductal factor responsible for converting the egg envelope to a sperm-penetrable form, via an increase in sperm binding. gp43 processing is the only requirement for envelope conversion
-
-
?
gp43 + H2O
gp41 + ?
-
preferential cleavage at Gly-Ser-Arg373-/-glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41. Processing of gp43 causes physical changes in the egg envelope which occurs during egg transit through the oxiduct
-
-
?
gp43 + H2O
gp41 + ?
-
preferential cleavage at Gly-Ser-Arg373-/-glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
it is proposed that hamster oviductin is a mucin-type glycoprotein which might act as a protective secretion influencing the first steps of the reproductive process necessary for the normal triggering of fertilization and early embryonic development
-
-
?
gp43 + H2O
gp41 + ?
oviductin alone is the oviductal factor responsible for converting the egg envelope to a sperm-penetrable form, via an increase in sperm binding. gp43 processing is the only requirement for envelope conversion
-
-
?
gp43 + H2O
gp41 + ?
-
preferential cleavage at Gly-Ser-Arg373-/-glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41. Processing of gp43 causes physical changes in the egg envelope which occurs during egg transit through the oxiduct
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
LiCl
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
NaCl
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
NaF
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
NaNO3
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no inhibition by iodoacetamide, E-64, pepstatin or 1,10-phenanthroline
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.058
Nalpha-tert-butoxycarbonylphenylalanylserylarginyl-7-amido-4-methylcoumarin
-
-
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.8
Nalpha-tert-butoxycarbonylphenylalanylserylarginyl-7-amido-4-methylcoumarin
-
-
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
Nalpha-tert-butoxycarbonylphenylalanylserylarginyl-4-methylcoumarin-7-amide
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 8.5
-
more than 90% of maximal activity at pH 7.5 and at pH 8.5, less than 30% of maximal activity below pH 6.5
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Rhinella arenarum, collected in Tucumán, Argentina, between May and October and housed at 25°C until used, gene OVCH2
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
endocytic compartments in the blastomeres of developing embryos
brenda
-
expressed in the chicken egg citelline membrane: using high-throughput, high-end LC-mass spectroscopy 137 proteins are identified. Specific components of the vitelline membrane not identified previously in other egg compartments include eight zona pellucida proteins, oviductin protease, and two ATPases
brenda
-
endocytic compartments in the blastomeres of developing embryos
brenda
-
negligible expression during the first three months of postnatal cervical differentiation. Transcripts are minimally detectable in the cervives of 4-month-old juveniles. Strong expression in the endocervices of adults is eliminated by ovariectomy and restored by estrogen treatment
brenda
-
after its release into the lumen of the oviduct, oviductin becomes associated with the zona pellucida of post-ovulatory oocytes. In unfertilized oocytes, oviductin is also detected in membrane invaginations along the oolemma and in some vesicles within multivesicular bodies
brenda
-
it is speculated that receptors for hamster oviductin-1 are present at the apical cell surface of endometrial cells and that implantation of the developing blastocyst into the uterine wall is possible only following downregulation of these receptors
brenda
-
oviductin is detected over the microvilli and within multivesicular bodies
brenda
additional information
-
expression of the oviductin gene is confined strictly to nonciliated secretory cells
brenda
-
hamster oviduction is inhibitory to in vitro fertilization, but oocytes with cumulus intact maintain their fertilizing capacity in the presence of oviductin
brenda
-
in Golgi saccules and secretory granules of the non-ciliated oviduct cells. After its release into the lumen, oviductin becomes associated with the zona pellucida of post-ovulatory oocytes
brenda
-
oviductin mRNA expression remains constant throughout the estrous cycle. Production of oviductin is not regulated differentially during the estrous cycle. The oviduct contains several forms of oviductin at each stage of the estrous cycle, the native glycosylated form(s) of 160350 kDa, and several precursor forms of 70100 kDa
brenda
-
oviductins are targeted to the oocyte via the interaction of their chitinase-like domains with specific oligosaccharide moieties of the zona pellucida. Once localized to this structure, oviductin molecules would act as a protective shield around the oocyte and early embryo by virtue of their densely glycosylated mucin-type domains
brenda
-
oviductins are targeted to the oocyte via the interaction of their chitinase-like domains with specific oligosaccharide moieties of the zona pellucida. Once localized to this structure, oviductin molecules would act as a protective shield around the oocyte and early embryo by virtue of their densely glycosylated mucin-type domains
brenda
-
some of the oviductin associated with the zona pellucida appears to be internalized by blastomeres of the embryo and further processed through the endosomal/lysosomal pathway
brenda
additional information
analysis of ovochymase 2 expression in the mouse reproductive tract, no expression in the oviduct
brenda
additional information
-
analysis of ovochymase 2 expression in the mouse reproductive tract, no expression in the oviduct
brenda
additional information
-
analysis of ovochymase 2 expression in the mouse reproductive tract, no expression in the oviduct
-
brenda
additional information
tissue expression analysis of oviductin
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
translational products stored in the pars recta granules need to be processed to become a proteolytically active 66000 Da form
brenda
-
in unfertilized oocytes, oviductin is detected in membrane invaginations along the oolemma and in some vesicles within multivesicular bodies
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
evolution
phylogenetic relationship between Bufo arenarum oviductin and Mus musculus ovochymase 2, overview
evolution
phylogenetic relationship between Bufo arenarum oviductin and Mus musculus ovochymase 2, overview. Protease gene families involved in reproduction and host defense played a role during the evolution of some mammalian species. Thus, the absence of ovochymase 2 RNA transcripts in oviduct might be one of the signs of the transition from a primitive fertilization mode (external fertilization) to a more complex form (internal fertilization)
evolution
-
phylogenetic relationship between Bufo arenarum oviductin and Mus musculus ovochymase 2, overview. Protease gene families involved in reproduction and host defense played a role during the evolution of some mammalian species. Thus, the absence of ovochymase 2 RNA transcripts in oviduct might be one of the signs of the transition from a primitive fertilization mode (external fertilization) to a more complex form (internal fertilization)
-
physiological function
oviductin, a serine protease with trypsin-like substrate specificity, hydrolyzes two kinds of egg envelope glycoproteins, gp84 and gp55, in the pars recta portion of the oviduct, thereby converting the egg to a penetrable state
physiological function
ovochymase 2 might produce proteolytic changes in the zona pellucida similar to the action of amphibian oviductin, which can play a role in embryo attachment to the uterine wall during implantation
physiological function
-
an anti-ovochymase antibody inhibits elevation of the vitelline coat at a late stage of oogenesis, during the period when selfsterility is acquired
physiological function
-
ovochymase 2 might produce proteolytic changes in the zona pellucida similar to the action of amphibian oviductin, which can play a role in embryo attachment to the uterine wall during implantation
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). OVCH2_BUFJA
974
0
107648
Swiss-Prot
Secretory Pathway (Reliability: 2)
OVCH2_RHIAE
980
0
108566
Swiss-Prot
Secretory Pathway (Reliability: 2)
OVCH2_XENLA
1004
0
110612
Swiss-Prot
Secretory Pathway (Reliability: 2)
E1AW56_MOUSE
152
0
16503
TrEMBL
other Location (Reliability: 3)
A0A6J8DP85_MYTCO
1007
0
111988
TrEMBL
Secretory Pathway (Reliability: 4)
A0A7R8CLG5_LEPSM
406
0
46273
TrEMBL
other Location (Reliability: 3)
A0A7R8CMJ3_LEPSM
212
0
23275
TrEMBL
Secretory Pathway (Reliability: 4)
A0A7R8CRD6_LEPSM
409
0
46609
TrEMBL
other Location (Reliability: 3)
A0A8B6D533_MYTGA
2222
0
249017
TrEMBL
other Location (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
oviductin is a multi-domain protein with a protease domain at the N-terminal region followed by two CUB domains and toward the C-terminal region another protease domain, which lacks an active histidine site, and one CUB domain
additional information
-
oviductin is a multi-domain protein with a protease domain at the N-terminal region followed by two CUB domains and toward the C-terminal region another protease domain, which lacks an active histidine site, and one CUB domain
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
-
contains terminal alpha-D-GalNAc and either terminal alpha-D-NeuAc or non-terminal beta-D-(GlcNAc)2 residues. Both the alpha- and beta-forms are sulphated on O-linked oligosaccharide side chains but are not phosphorylated. The hamster oviductin polymorphism is a consequence of different glycosylation patterns and not the polypeptide chain itself. Hamster oviductin is mostly O-glycosylated and contains a few N-linked oligosaccharide side chains (approx. 10 kDa). It is proposed that hamster oviductin is a mucin-type glycoprotein which might act as a protective secretion influencing the first steps of the reproductive process necessary for the normal triggering of fertilization and early embryonic development
glycoprotein
-
glycosylation of hamster oviductin appears to be differentially regulated during the estrous cycle
glycoprotein
-
polymorphism in the heavily O-glycosylated region of hamster oviductin
glycoprotein
-
the mature MOGP contained three potential N-linked glycosylation sites and 24 possible O-linked glycosylation sites
glycoprotein
-
the mature MOGP contained three potential N-linked glycosylation sites and 24 possible O-linked glycosylation sites
-
proteolytic modification
translational products stored in the pars recta granules need to be processed to become a proteolytically active 66000 Da form. Extensive posttranslational processing for activation of proteolytic activity. Oviductin translated as 107.6-kDa precursors are processed both N- and C-terminally to give rise to a 66-kDa active form comprising a serine protease and two CUB domains
proteolytic modification
protease is translated as the N terminus of an unusual mosaic protein. It is proposed that during post-translational proteolytic processing of the mosaic oviductin glycoprotein, the processed N-terminal protease domain is released coupled to two C-terminal CUB domains and constitutes the enzymatically active protease molecule
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
relatively stable to rapid freezing in the presence of 20% glycerol. 90% of the activity remains after each freeze-thaw cycle
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene OVCH2, DNA and amino acid sequence determination and analysis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Malette, B.; Bleau, G.
Biochemical characterization of hamster oviductin as a sulphated zona pellucida-binding glycoprotein
Biochem. J.
295
437-445
1993
Mesocricetus auratus
brenda
Hardy, D.M.; Hedrick, J.L.
Oviductin. Purification and properties of the oviductal protease that processes the molecular weight 43000 glycoprotein of the Xenopus laevis egg envelope
Biochemistry
31
4466-4472
1992
Xenopus laevis
brenda
Kan, F.W.; Roux, E.; Bleau, G.
Immunolocalization of oviductin in endocytic compartments in the blastomeres of developing embryos in the golden hamster
Biol. Reprod.
48
77-88
1993
Mesocricetus auratus
brenda
Malette, B.; Paquette, Y.; Bleau, G.
Size variations in the mucin-type domain of hamster oviductin: identification of the polypeptide precursors and characterization of their biosynthetic maturation
Biol. Reprod.
53
1311-1323
1995
Mesocricetus auratus
brenda
Sendai, Y.; Komiya, H.; Suzuki, K.; Onuma, T.; Kikuchi, M.; Hoshi, H.; Araki, Y.
Molecular cloning and characterization of a mouse oviduct-specific glycoprotein
Biol. Reprod.
53
285-294
1995
Mus musculus, Mus musculus ICR
brenda
Lindsay, L.L.; Wieduwilt, M.J.; Hedrick, J.L.
Oviductin, the Xenopus laevis oviductal protease that processes egg envelope glycoprotein gp43, increases sperm binding to envelopes, and is translated as part of an unusual mosaic protein composed of two protease and several CUB domains
Biol. Reprod.
60
989-995
1999
Xenopus laevis (P79953), Xenopus laevis
brenda
McBride, D.S.; Boisvert, C.; Bleau, G.; Kan, F.W.
Evidence for the regulation of glycosylation of golden hamster (Mesocricetus auratus) oviductin during the estrous cycle
Biol. Reprod.
70
198-203
2004
Mesocricetus auratus
brenda
Hiyoshi, M.; Takamune, K.; Mita, K.; Kubo, H.; Sugimoto, Y.; Katagiri, C.
Oviductin, the oviductal protease that mediates gamete interaction by affecting the vitelline coat in Bufo japonicus: its molecular cloning and analyses of expression and posttranslational activation
Dev. Biol.
243
176-184
2002
Bufo japonicus (Q90WD8), Bufo japonicus
brenda
Hendrix, E.; Hewetson, A.; Mansharamani, M.; Chilton, B.S.
Oviductin (Muc9) is expressed in rabbit endocervix
Endocrinology
142
2151
2001
Oryctolagus cuniculus
brenda
Wagh, P.V.; Lippes, J.
Human oviductal fluid proteins. V. Identification of human oviductin-I as alpha-fetoprotein
Fertil. Steril.
59
148-156
1993
Homo sapiens
brenda
Ling, L.; Lee, Y.L.; Lee, K.F.; Tsao, S.W.; Yeung, W.S.; Kan, F.W.
Expression of human oviductin in an immortalized human oviductal cell line
Fertil. Steril.
84 Suppl 2
1095-1103
2005
Homo sapiens
brenda
Martoglio, A.M.; Kan, F.W.
Immunohistochemical localization of oviductin in the endometrial lining of the golden hamster (Mesocricetus auratus) during the estrous cycle and early gestation
Histochem. J.
28
449-459
1996
Mesocricetus auratus
brenda
Llanos, R.J.; Barrera, D.; Valz-Gianinet, J.N.; Miceli, D.C.
Oviductal protease and trypsin treatment enhance sperm-envelope interaction in Bufo arenarum coelomic eggs
J. Exp. Zool. A
305
872-882
2006
Rhinella arenarum
brenda
McBride, D.S.; Boisvert, C.; Bleau, G.; Kan, F.W.
Detection of nascent and/or mature forms of oviductin in the female reproductive tract and post-ovulatory oocytes by use of a polyclonal antibody against recombinant hamster oviductin
J. Histochem. Cytochem.
52
1001-1009
2004
Mesocricetus auratus
brenda
Kimura, H.; Matsuda, J.; Ogura, A.; Asano, T.; Naiki, M.
Affinity binding of hamster oviductin to spermatozoa and its influence on in vitro fertilization
Mol. Reprod. Dev.
39
322-327
1994
Mesocricetus auratus
brenda
Malette, B.; Paquette, Y.; Merlen, Y.; Bleau, G.
Oviductins possess chitinase- and mucin-like domains: a lead in the search for the biological function of these oviduct-specific ZP-associating glycoproteins
Mol. Reprod. Dev.
41
384-397
1995
Bos taurus, Oryctolagus cuniculus, Ovis aries, Homo sapiens, Mesocricetus auratus, Mus musculus, Papio hamadryas, Sus scrofa
brenda
Merlen, Y.; Bleau, G.
Organization of a gene coding for an oviduct-specific glycoprotein (oviductin) in the hamster
Mol. Reprod. Dev.
57
238-246
2000
Mesocricetus auratus
brenda
Mann, K.
Proteomic analysis of the chicken egg vitelline membrane
Proteomics
8
2322-2332
2008
Gallus gallus
brenda
Mugnier, S.; Kervella, M.; Douet, C.; Canepa, S.; Pascal, G.; Deleuze, S.; Duchamp, G.; Monget, P.; Goudet, G.
The secretions of oviduct epithelial cells increase the equine in vitro fertilization rate: are osteopontin, atrial natriuretic peptide A and oviductin involved?
Reprod. Biol. Endocrinol.
7
129
2009
Bos taurus, Equus caballus
brenda
Barrera, D.; Valdecantos, P.; Garcia, E.; Miceli, D.
Cloning and sequence analysis of Bufo arenarum oviductin cDNA and detection of its orthologous gene expression in the mouse female reproductive tract
Zygote
20
17-26
2012
Mus musculus (Q7M761), Mus musculus, Mus musculus BALB/c (Q7M761), Rhinella arenarum (Q66TN7), Rhinella arenarum
brenda
Mino, M.; Sawada, H.
Follicle cell trypsin-like protease HrOvochymase Its cDNA cloning, localization, and involvement in the late stage of oogenesis in the ascidian Halocynthia roretzi
Mol. Reprod. Dev.
83
347-358
2016
Halocynthia roretzi
brenda
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